The evolution of paramagnetic NMR as a tool in structural biology-Reference-Cited by-同舟云学术

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The evolution of paramagnetic NMR as a tool in structural biology

Published:2022 Issue:29 Volume:24 Page:17397-17416
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Ravera Enrico¹²³^ORCID,Gigli Lucia¹²³^ORCID,Fiorucci Letizia¹²³^ORCID,Luchinat Claudio¹²³^ORCID,Parigi Giacomo¹²³^ORCID

Affiliation:

1. Magnetic Resonance Center (CERM), University of Florence, via Luigi Sacconi 6, Sesto Fiorentino, 50019, Italy

2. Department of Chemistry “Ugo Schiff”, University of Florence, via della Lastruccia 3, Sesto Fiorentino, 50019, Italy

3. Consorzio Interuniversitario Risonanze Magnetiche Metallo Proteine (CIRMMP), via Luigi Sacconi 6, Sesto Fiorentino, 50019, Italy

Abstract

Paramagnetic NMR observables provide accurate long-range structural information and act as a loupe on the metal coordination site.

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2022/CP/D2CP01838A

Reference150 articles.

1. In-Cell NMR in Human Cells: Direct Protein Expression Allows Structural Studies of Protein Folding and Maturation

2. The Solution Structure Refinement of the Paramagnetic Reduced High-Potential Iron-Sulfur Protein I from Ectothiorhodospira Halophila by Using Stable Isotope Labeling and Nuclear Relaxation

3. The use of pseudocontact shifts to refine solution structures of paramagnetic metalloproteins: Met80Ala cyano-cytochrome c as an example

4. Partial Orientation of Oxidized and Reduced Cytochrome b5 at High Magnetic Fields: Magnetic Susceptibility Anisotropy Contributions and Consequences for Protein Solution Structure Determination

5. Nuclear magnetic dipole interactions in field-oriented proteins: information for structure determination in solution.

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